ID T1ZDK3_STRIT Unreviewed; 809 AA.
AC T1ZDK3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:AGU75527.1};
GN Name=clpC {ECO:0000313|EMBL:AGU75527.1};
GN ORFNames=SIR_0133 {ECO:0000313|EMBL:AGU75527.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU75527.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU75527.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU75527.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP003857; AGU75527.1; -; Genomic_DNA.
DR RefSeq; WP_021002326.1; NZ_UZBH01000004.1.
DR AlphaFoldDB; T1ZDK3; -.
DR KEGG; sib:SIR_0133; -.
DR PATRIC; fig|862967.3.peg.114; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000016233; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:AGU75527.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AGU75527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 809 AA; 90125 MW; 736E6581ADC2B303 CRC64;
MKYSKALTES IESAQLLASH FETDYLESWQ LLIAMANNPY SVAGSVLNDY PLEIDDFEKA
AFHITGKVYQ QEGDFTIWPF SYRMKVLFLT AEQIAGAVHA NNLGTEHILL AMLFDRGSLA
ARILEFIGFS YEDKEGVLRM TDLRKNLEHK ASWNKEDLKA IRHLNKSAAA TRQTMANMMG
MPPATSGGLE DYTRDLTEMA HMGLLEPVIG RDKEISRILQ ILSRKTKNNP VLVGDAGVGK
TALALGLAQR VADGQVPNEL AKMRVLELDL MNVVAGTRFR GDFEERMNNI INDIEADGHV
ILFIDELHTI MGSGSGIDST LDAANILKPA LAKGTLRTIG ATTQEEYQKY IEKDAALSRR
FAKVTIEEPT VADSIAILQG LKKSYEDHHK VVITDSAIET AVKYAHRYLT SKHLPDSAID
LLDEAAARVQ NKSPQNHVKA ELSAADEALM AGDWNKVDTL LEKESQPIVY KLRVKDEDVL
ATLSSLSGIP VQKLTQTDAK KYLNLEKELH KRVIGQNEAI SAISRAIRRN QSGIRTSKRP
IGSFLFLGPT GVGKTELAKA LAEVLFDDET ALIRFDMSEY MEKFAASRLN GAPPGYVGYE
EGGELTEKVR NRPYSVLLFD EVEKAHPDIF NVLLQVLDDG VLTDSKGRKV DFSNTIIIMT
SNLGATSLRD DKTVGFGARD VRFDHENMEK RMMEELKKAY RPEFINRIDE KVVFHSLTSE
DMQEVVKIMV QPLISSLAEK GIKLKFQPSA LKLLAQEGYD PEMGARPLRR ILQTRVEDHL
SELLLSGELK MGQSLKVGVK AGKLKFEVL
//
